Protein Stability The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation is only meaningful for the polar amino acids reflects the reduction in solvent-accessible area during protein folding ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Attractive Vander Waals forces occur between only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state polar molecules in the solid state only if other forces are less favorable any pair of nearby atoms apolar molecules in the liquid state polar molecules in the solid state ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold increase in K decreases ΔG° by about 10-fold ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most favorable for protein folding? Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds Conformational entropy Vander Waals interactions Hydrophobic Interactions Hydrogen bonds ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following forces is the most unfavorable for protein folding? Hydrophobic interactions Electrostatic interactions Conformational entropy Vander Waals interactions Hydrophobic interactions Electrostatic interactions Conformational entropy Vander Waals interactions ANSWER DOWNLOAD EXAMIANS APP
Protein Stability At the midpoint of a temperature transition curve, Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] All of these half of the protein is denatured Keq = 1.0 and ΔG = 0 [Native] = [Unfolded] All of these half of the protein is denatured ANSWER DOWNLOAD EXAMIANS APP
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